The effects of temperature and ionic strength on the formation of the hydroxide complex of ferric horseradish peroxidase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Untersuchungen an künstlichen Peroxydasen.
2. Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin
3. OXIDATION-REDUCTION POTENTIALS OF HORSERADISH PEROXIDASE
4. The Electronic Structure of Protoheme Proteins
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1. Coordination geometry of heme, in lactoperoxidase. pH-Dependent 1H relaxivity and optical spectral studies;Journal of Inorganic Biochemistry;1990-01
2. Oxygen-17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases.;Journal of Biological Chemistry;1988-11
3. Resonance Raman spectroscopic evidence for heme iron-hydroxide ligation in peroxidase alkaline forms.;Journal of Biological Chemistry;1988-09
4. Resonance Raman spectroscopic characterizations of horseradish peroxidase. Observations of the FeIV = O stretching vibration of Compound II;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1985-03
5. Physicochemical characterization of the alkaline denaturation of cytochrome c proxidase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1985-02
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